We wish to contribute to an elucidation of the major pathways in which multiply coupled aggregating systems react chemically subsequent to small physical perturbations. In the case of self-aggregating or spontaneously dissociating systems such as represented by the hemocyanins or E. coli ribosomes, there is some evidence from temperature-jump light-scattering measurements that an initial diffusion-controlled process produces a transient aggregated intermediate, which then rearranges in a relatively slow process. The early stages of temperature-jump measurements are complicated not only by non-specific refractive index shifts, but also by mutual inductance effects which become very troublesome at the low levels of scattered light. Most investigators have shunted out their detecting system during the heating period, and have entirely missed processes which occur during this period or immediately afterward. With the pressure-jump methods refractive index effects still exist, but troublesome spurious electrical effects are eliminated. Through the use of a modified Hoffman and Yeager shock-tube pressure-jump technique, with 90 degrees scattered light for detection, we hope to gain access to the time domain of all intermolecular processes taking place in protein aggregation. For classical micelle systems, we have proposed a model for the redistribution of species in relaxation processes, which may be amenable to direct test with such equipment. In the case of ribosomes, recycling of protein synthesis involves directly the association-dissociation process as one part of the total mechanism. In the case of micellar systems, a detailed knowledge of self-aggregation pathways would furnish a helpful basis for the further understanding of solubilization and transport phenomena involved in natural processes or in pharmaceutical applications.